Related Experiment Video
Updated: Jun 15, 2026

Reconstitution of Msp1 Extraction Activity with Fully Purified Components
Published on: August 10, 2021
The structure of Get4 reveals an alpha-solenoid fold adapted for multiple interactions in tail-anchored protein
Gunes Bozkurt1, Klemens Wild, Stefan Amlacher
1Heidelberg University Biochemistry Center (BZH), Heidelberg, Germany.
Abstract:
Tail-anchored proteins play important roles in protein translocation, membrane fusion and apoptosis. They are targeted to the endoplasmic reticulum membrane via the guided-entry of tail-anchored proteins (Get) pathway. We present the 2A crystal structure of Get4 which participates in early steps of the Get pathway. The structure shows an alpha-solenoid fold with particular deviations from the regular pairwise arrangement of alpha-helices. A conserved hydrophobic groove accommodates the flexible C-terminal region in trans. The structural organization of the Get4 helical hairpin motifs provides a scaffold for protein-protein interactions in the Get pathway.
Related Concept Videos
Protein Folding
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding
Tail-anchoring of Proteins in the ER Membrane
Protein Organization
Protein Organization
The primary structure of a protein is its amino acid sequence.

